ID A5ZYB9_9FIRM Unreviewed; 429 AA.
AC A5ZYB9;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=L-aspartate oxidase {ECO:0000256|ARBA:ARBA00012173};
DE EC=1.4.3.16 {ECO:0000256|ARBA:ARBA00012173};
DE AltName: Full=Quinolinate synthase B {ECO:0000256|ARBA:ARBA00030386};
GN ORFNames=RUMOBE_04028 {ECO:0000313|EMBL:EDM85396.1};
OS Blautia obeum ATCC 29174.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=411459 {ECO:0000313|EMBL:EDM85396.1, ECO:0000313|Proteomes:UP000006002};
RN [1] {ECO:0000313|EMBL:EDM85396.1, ECO:0000313|Proteomes:UP000006002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29174 {ECO:0000313|EMBL:EDM85396.1,
RC ECO:0000313|Proteomes:UP000006002};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDM85396.1, ECO:0000313|Proteomes:UP000006002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29174 {ECO:0000313|EMBL:EDM85396.1,
RC ECO:0000313|Proteomes:UP000006002};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus obeum (ATCC 29174).";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate + O2 = H2O2 + iminosuccinate;
CC Xref=Rhea:RHEA:25876, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:77875; EC=1.4.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00029281};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25877;
CC Evidence={ECO:0000256|ARBA:ARBA00029281};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate
CC from L-aspartate (oxidase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004950}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB
CC subfamily. {ECO:0000256|ARBA:ARBA00008562}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDM85396.1}.
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DR EMBL; AAVO02000033; EDM85396.1; -; Genomic_DNA.
DR RefSeq; WP_005425487.1; NZ_DS264322.1.
DR AlphaFoldDB; A5ZYB9; -.
DR GeneID; 79803013; -.
DR eggNOG; COG0029; Bacteria.
DR HOGENOM; CLU_014312_3_1_9; -.
DR UniPathway; UPA00253; UER00326.
DR Proteomes; UP000006002; Unassembled WGS sequence.
DR GO; GO:0008734; F:L-aspartate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0044318; F:L-aspartate:fumarate oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR005288; NadB.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR PANTHER; PTHR42716; L-ASPARTATE OXIDASE; 1.
DR PANTHER; PTHR42716:SF2; L-ASPARTATE OXIDASE, CHLOROPLASTIC; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642}.
FT DOMAIN 6..370
FT /note="FAD-dependent oxidoreductase 2 FAD binding"
FT /evidence="ECO:0000259|Pfam:PF00890"
SQ SEQUENCE 429 AA; 48448 MW; 1B9494C18E7C2636 CRC64;
MKENYDVIIV GTGAAGLYCA LNLPSRMKVL MLTKQQADQS DSFLAQGGIC MLRGEEDYND
YFEDTMRAGH YENDAKAVEL MIRSSNSIIR DLLQRNVTFE RTETGELDFT REGAHSQPRI
LFYEDITGKQ ITQTLLNQAL TRDNIEICEY MTMVDIISKD NVCGGVIVMD EKNEVYPVRA
PYVVLACGGL GGLYKNSTNF PHIAGDGLGI AMKHQVVLEH LDYIQIHPTT LYSHKPGRRF
LISESVRGEG ALLYDKNGQR FTNELQPRDL LSQAIFAQME KDGTDFVWED MRPLGEETIM
KHFPNIFHRC VEEGFDPRKE PIPVVPAQHY FMGGIKVDLG SRTSMKGLYA CGETSCNGVH
GKNRLASNSL LESLVFARRA ADDIIFGRKP DPCRPGSIDL KPYEDRDAVL TVYHEMVLNE
IERMKKSHE
//
